Sequence-specific ^sup 1^H, ^sup 13^C and ^sup 15^N assignments of the phosphoesterase (PE) domain of Pseudomonas aeruginosa DNA ligase D (LigD)

DNA ligase D (LigD), consisting of polymerase, ligase and phosphoesterase domains, is the essential catalyst of the bacterial non-homologous end-joining pathway of DNA double-strand break repair. The phosphoesterase (PE) module performs manganese-dependent 3'-phosphomonoesterase and 3'-rib...

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Veröffentlicht in:Biomolecular NMR assignments 2011-10, Vol.5 (2), p.151
Hauptverfasser: Dutta, Kaushik, Natarajan, Aswin, Nair, Pravin A, Shuman, Stewart, Ghose, Ranajeet
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Sprache:eng
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Zusammenfassung:DNA ligase D (LigD), consisting of polymerase, ligase and phosphoesterase domains, is the essential catalyst of the bacterial non-homologous end-joining pathway of DNA double-strand break repair. The phosphoesterase (PE) module performs manganese-dependent 3'-phosphomonoesterase and 3'-ribonucleoside resection reactions that heal broken ends in preparation for sealing. LigD PE exemplifies a structurally and mechanistically unique class of DNA end-processing enzymes. Here, we present the resonance assignments of the PE domain of Pseudomonas aeruginosa LigD comprising the N-terminal 177 residues.[PUBLICATION ABSTRACT]
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-010-9289-7